Primary Information |
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| BoMiProt ID | Bomi4814 |
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| Protein Name | Collagen alpha-2(I) chain/Alpha-2 type I collagen |
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| Organism | Bos taurus |
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| Uniprot ID | P02465 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776945.1 |
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| Aminoacid Length | 1364 |
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| Molecular Weight | 129064 |
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| FASTA Sequence |
Download |
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| Gene Name | COL1A2 |
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| Gene ID | 282188 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | ECM component,responsible for ECM assembly.Type ! Collagen is composed of two α1 chains and one α2 chain encoded by two distinct genes, type I α1 collagen (COL1A1) and type I α2 collagen (COL1A2).major producer of collagen type I in the fibrotic liver. |
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| PTMs | Disulfide bond formation, Glycosylation, Hydroxylation, Pyrrolidone carboxylic acid addition. |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P02465|CO1A2_BOVIN Collagen alpha-2(I) chain OS=Bos taurus OX=9913 GN=COL1A2 PE=1 SV=2
MLSFVDTRTLLLLAVTSCLATCQSLQEATARKGPSGDRGPRGERGPPGPPGRDGDDGIPG
PPGPPGPPGPPGLGGNFAAQFDAKGGGPGPMGLMGPRGPPGASGAPGPQGFQGPPGEPGE
PGQTGPAGARGPPGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFK*175GIRGH
NGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGP
VGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGA
NGLPGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGE
PGAVGQPGPPGPSGEEGKRGSTGEIGPAGPPGPPGLRGNPGSRGLPGADGRAGVMGPAGS
RGATGPAGVRGPNGDSGRPGEPGLMGPRGFPGSPGNIGPAGKEGPVGLPGIDGRPGPIGP
AGARGEPGNIGFPGPKGPSGDPGKAGEKGHAGLAGARGAPGPDGNNGAQGPPGLQGVQGG
KGEQGPAGPPGFQGLPGPAGTAGEAGKPGERGIPGEFGLPGPAGARGERGPPGESGAAGP
TGPIGSRGPSGPPGPDGNKGEPGVVGAPGTAGPSGPSGLPGERGAAGIPGGKGEKGETGL
RGDIGSPGRDGARGAPGAIGAPGPAGANGDRGEAGPAGPAGPAGPRGSPGERGEVGPAGP
NGFAGPAGAAGQPGAKGERGTKGPKGENGPVGPTGPVGAAGPSGPNGPPGPAGSRGDGGP
PGATGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRSGETGASGPPGF
VGEKGPSGEPGTAGPPGTPGPQGLLGAPGFLGLPGSRGERGLPGVAGSVGEPGPLGIAGP
PGARGPPGNVGNPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNAGPVGAAGA
PGPQGPVGPVGKHGNRGEPGPAGAVGPAGAVGPRGPSGPQGIRGDKGEPGDKGPRGLPGL
KGHNGLQGLPGLAGHHGDQGAPGAVGPAGPRGPAGPSGPAGKDGRIGQPGAVGPAGIRGS
QGSQGPAGPPGPPGPPGPPGPSGGGYEFGFDGDFYRADQPRSPTSLRPKDYEVDATLKSL
NNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGET
CIRAQPEDIPVKNWYRNSKAKKHVWVGETINGGTQFEYNVEGVTTKEMATQLAFMRLLAN
HASQN*1265ITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTN
EWQKTIIEYKTNKPSRLPILDIAPLDIGGADQEIRLNIGPVCFK
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Hydroxylation of proline and lysine occurs only in the Y-position of the triplet Gly-X-Y. |
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| Bibliography | 1.Fietzek PP, Rexrodt FW. The covalent structure of collagen. The amino-acid sequence of alpha2-CB4 from calf-skin collagen. Eur J Biochem. 1975 Nov 1;59(1):113-8. doi: 10.1111/j.1432-1033.1975.tb02431.x. PMID: 173531. 2.Zhao Y, Shi X, Ding C, Feng D, Li Y, Hu Y, Wang L, Gao D, Tian X, Yao J. Carnosic acid prevents COL1A2 transcription through the reduction of Smad3 acetylation via the AMPKα1/SIRT1 pathway. Toxicol Appl Pharmacol. 2018 Jan 15;339:172-180. doi: 10.1016/j.taap.2017.12.010. Epub 2017 Dec 15. PMID: 29253500. |
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